Plant-derived cysteine proteases have emerged as a compelling subject of investigation, capturing scientific interest owing to their potential applications in diverse industries, including food and biotechnology. This study focused on isolating Kaempferia galanga cysteine protease (KgCP) from rhizomes of Kaempferia galanga, followed by a comprehensive characterization of the protease. It was purified and characterized using various biochemical and biophysical techniques, including anion-exchange chromatography, gel filtration, SDS-PAGE electrophoresis, and enzyme assays. With a yield of 23.2%, the purification process generated a 6.03-fold increase in specific activity. KgCP's molecular weight was determined to be around 33 kDa and exhibited optimal catalytic performance at 55 °C and pH 5.5. Values of its catalytic parameters, V